Bacterial usurpation of the OTU deubiquitinase fold

被引:2
作者
Pruneda, Jonathan N. N. [1 ]
Nguyen, Justine V. V. [1 ]
Nagai, Hiroki [2 ,3 ]
Kubori, Tomoko [2 ]
机构
[1] Oregon Hlth & Science Univ, Dept Mol Microbiol &Immunol, Portland, OR 97239 USA
[2] Gifu Univ, Grad Sch Med, Dept Microbiol, Gifu 5011194, Japan
[3] Gifu Univ, Inst Adv Study, Ctr One Med Innovat Translat Res, Gifu, Japan
关键词
bacteria; deubiquitinase; infection; OTU; protein prediction; structure; ubiquitin; PNEUMOPHILA REPLICATION VACUOLE; LEGIONELLA-PNEUMOPHILA; CYSTEINE PROTEASES; UBIQUITIN LIGASES; PLASMA-MEMBRANE; MOLECULAR-BASIS; ASSOCIATION; PHAGOSOME; ENZYMES; EXPLOITATION;
D O I
10.1111/febs.16725
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The extensive cellular signalling events controlled by posttranslational ubiquitination are tightly regulated through the action of specialized proteases termed deubiquitinases. Among them, the OTU family of deubiquitinases can play very specialized roles in the regulation of discrete subtypes of ubiquitin signals that control specific cellular functions. To exert control over host cellular functions, some pathogenic bacteria have usurped the OTU deubiquitinase fold as a secreted virulence factor that interferes with ubiquitination inside infected cells. Herein, we provide a review of the function of bacterial OTU deubiquitinases during infection, the structural basis for their deubiquitinase activities and the bioinformatic approaches leading to their identification. Understanding bacterial OTU deubiquitinases holds the potential for discoveries not only in bacterial pathogenesis but in eukaryotic biology as well.
引用
收藏
页码:3303 / 3316
页数:14
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